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We are analyzing https://link.springer.com/article/10.1007/s00436-014-4060-0.

Title:
Plasmodium knowlesi thioredoxin peroxidase 1 binds to nucleic acids and has RNA chaperone activity | Parasitology Research
Description:
Malaria parasites are under oxidative attack throughout their life cycle in human body and mosquito vector. Therefore, Plasmodium antioxidant defenses are crucial for its survival and being considered as interesting target for antimalarial drug design. Plasmodium knowlesi has emerged recently from its simian host to human in Southeast Asia and has been recognized as the fifth Plasmodium species that can cause human malaria. In this study, we cloned and characterized thioredoxin peroxidase 1 from P. knowlesi (PkTPx-1). PkTPx-1 gene was cloned, and recombinant protein was produced by heterologous overexpression in Escherichia coli. The recombinant protein was used for evaluation of enzymatic activity and polyclonal antibody production. Using the recombinant PkTPx-1 protein, its antioxidant activity was confirmed in a mixed-function oxidation assay where PkTPx-1 prevented nicking of DNA by hydroxyl radicals. PkTPx-1 was able to bind to double-strand DNA and RNA and had RNA chaperone activity in a nucleic acid melting assay indicating new function of PkTPx-1 other than antioxidant activity. Using specific polyclonal antibodies, it was indicated that PkTPx-1 is expressed in the cytoplasm of the parasite. Altogether, these results suggest that PkTPx-1 not only protects the parasite from the adverse effects of reactive oxygen species but also has RNA chaperone activity.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
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Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

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🌠 Phenomenal Traffic: 5M - 10M visitors per month


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How Does Link.springer.com Make Money? {💸}

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Keywords {🔍}

article, pubmed, google, scholar, cas, plasmodium, activity, knowlesi, rna, chaperone, malaria, pktpx, peroxiredoxin, kawazu, parasite, parasitol, kim, research, lee, thioredoxin, peroxidase, nucleic, hakimi, human, antioxidant, access, falciparum, proteins, res, privacy, cookies, content, angeles, protein, biochem, int, central, peroxiredoxins, function, publish, search, asada, inoue, recombinant, redox, cys, dois, rhee, japan, author,

Topics {✒️}

month download article/chapter rna-binding properties crucial peroxidase-unrelated role nucleic acid melting malaria parasite-infected erythrocytes shin-ichiro kawazu mixed-function oxidation assay 2-cys peroxiredoxin pftrx-px1 rna chaperone activity full article pdf typical 2-cys peroxiredoxins—structures jose ma privacy choices/manage cookies related subjects rhee sg jang hh article hakimi diverse proteins human malaria parasite life cycle molecular chaperone function plasmodium antioxidant defenses host–parasite interactions european economic area antimalarial drug design polyclonal antibody production specific polyclonal antibodies ferreira-da-silva intracellular messenger h2o2 genome-wide chromatin common task-impediment electronic supplementary material plasmodium knowlesi conditions privacy policy scientific research reactive oxygen species dokkyo medical university article log hirono masuda-suganuma redox-sensitive oligomerization author information authors proteins plasmodium falciparum accepting optional cookies double-strand dna escherichia coli cspe article cite chaperone activity check access instant access

Schema {🗺️}

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         headline:Plasmodium knowlesi thioredoxin peroxidase 1 binds to nucleic acids and has RNA chaperone activity
         description:Malaria parasites are under oxidative attack throughout their life cycle in human body and mosquito vector. Therefore, Plasmodium antioxidant defenses are crucial for its survival and being considered as interesting target for antimalarial drug design. Plasmodium knowlesi has emerged recently from its simian host to human in Southeast Asia and has been recognized as the fifth Plasmodium species that can cause human malaria. In this study, we cloned and characterized thioredoxin peroxidase 1 from P. knowlesi (PkTPx-1). PkTPx-1 gene was cloned, and recombinant protein was produced by heterologous overexpression in Escherichia coli. The recombinant protein was used for evaluation of enzymatic activity and polyclonal antibody production. Using the recombinant PkTPx-1 protein, its antioxidant activity was confirmed in a mixed-function oxidation assay where PkTPx-1 prevented nicking of DNA by hydroxyl radicals. PkTPx-1 was able to bind to double-strand DNA and RNA and had RNA chaperone activity in a nucleic acid melting assay indicating new function of PkTPx-1 other than antioxidant activity. Using specific polyclonal antibodies, it was indicated that PkTPx-1 is expressed in the cytoplasm of the parasite. Altogether, these results suggest that PkTPx-1 not only protects the parasite from the adverse effects of reactive oxygen species but also has RNA chaperone activity.
         datePublished:2014-08-05T00:00:00Z
         dateModified:2014-08-05T00:00:00Z
         pageStart:3957
         pageEnd:3962
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             Plasmodium knowlesi
            Thioredoxin peroxidase 1
            Nucleic acid binding
            RNA chaperone
            Medical Microbiology
            Microbiology
            Immunology
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      headline:Plasmodium knowlesi thioredoxin peroxidase 1 binds to nucleic acids and has RNA chaperone activity
      description:Malaria parasites are under oxidative attack throughout their life cycle in human body and mosquito vector. Therefore, Plasmodium antioxidant defenses are crucial for its survival and being considered as interesting target for antimalarial drug design. Plasmodium knowlesi has emerged recently from its simian host to human in Southeast Asia and has been recognized as the fifth Plasmodium species that can cause human malaria. In this study, we cloned and characterized thioredoxin peroxidase 1 from P. knowlesi (PkTPx-1). PkTPx-1 gene was cloned, and recombinant protein was produced by heterologous overexpression in Escherichia coli. The recombinant protein was used for evaluation of enzymatic activity and polyclonal antibody production. Using the recombinant PkTPx-1 protein, its antioxidant activity was confirmed in a mixed-function oxidation assay where PkTPx-1 prevented nicking of DNA by hydroxyl radicals. PkTPx-1 was able to bind to double-strand DNA and RNA and had RNA chaperone activity in a nucleic acid melting assay indicating new function of PkTPx-1 other than antioxidant activity. Using specific polyclonal antibodies, it was indicated that PkTPx-1 is expressed in the cytoplasm of the parasite. Altogether, these results suggest that PkTPx-1 not only protects the parasite from the adverse effects of reactive oxygen species but also has RNA chaperone activity.
      datePublished:2014-08-05T00:00:00Z
      dateModified:2014-08-05T00:00:00Z
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          Plasmodium knowlesi
         Thioredoxin peroxidase 1
         Nucleic acid binding
         RNA chaperone
         Medical Microbiology
         Microbiology
         Immunology
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      name:National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Japan
      name:National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Japan
      name:National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Japan
      name:National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Japan
      name:Department of Protozoology, Institute of Tropical Medicine (NEKKEN), Nagasaki University, Nagasaki, Japan
      name:Laboratory of Tropical Medicine and Parasitology, Dokkyo Medical University, Mibu, Japan
      name:National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Japan
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External Links {🔗}(143)

Analytics and Tracking {📊}

  • Google Tag Manager

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  • Clipboard.js
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  • Crossref

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